کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
4011557 | 1602625 | 2010 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Aggregation of deamidated human βB2-crystallin and incomplete rescue by α-crystallin chaperone
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
DLSDSCSAXSPMSFIPTGβ-crystallins - β-کریستالین هاcataracts - آب مرواریدSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدSodium dodecyl sulfate polyacrylamide gel electrophoresis - الکتروفورز ژل پلی اتیل آمید سدیم دودسیل سولفاتFörster resonance energy transfer - انتقال انرژی تابشی ForsterFRET - انتقال انرژی رزونانسی فورسترDeamidation - انحلالprotein aggregation - تجمع پروتئینMolecular mass - توده مولکولیthree dimensional - سه بعدیRadius of gyration - شعاع نفوذHydrodynamic radius - شعاع هیدرودینامیکیLens - عدسی یا لنز Molecular weight - وزن مولکولیsmall angle X-ray Scattering - پراکندگی اشعه ایکس زاویه کوچکDynamic Light Scattering - پراکندگی نور دینامیکیPolydispersity - پلیدرزاییDifferential scanning calorimetry - کالریمتری روبشی افتراقی
موضوعات مرتبط
علوم زیستی و بیوفناوری
ایمنی شناسی و میکروب شناسی
ایمونولوژی و میکروب شناسی (عمومی)
پیش نمایش صفحه اول مقاله

چکیده انگلیسی
Aging of the lens is accompanied by extensive deamidation of the lens specific proteins, the crystallins. Deamidated crystallins are increased in the insoluble proteins and may contribute to cataracts. Deamidation has been shown in vitro to alter the structure and decrease the stability of human lens βB1, βB2 and βA3-crystallin. Of particular interest, βB2 mutants were constructed to mimic the effect of in vivo deamidations at the interacting interface between domains, at Q70 in the N terminal domain and at Q162, its C-terminal homologue. The double mutant was also constructed. We previously reported that deamidation at the critical interface sites decreased stability, while preserving the dimeric 3D structure. In the present study, dynamic light scattering, differential scanning calorimetry and small angle X-ray scattering were used to investigate the effect of deamidation on stability, thermal unfolding and aggregation. The bovine βLb fraction was used for comparative analysis. The chaperone requirements of the various samples were determined using bovine α-crystallins as the chaperone. Deamidation at both interface Gln residues or at Q70, but not Q162, significantly lowered the temperature for unfolding and aggregation, which was rapidly followed by precipitation. This deamidation-induced aggregation and precipitation was not completely prevented by α-crystallin chaperone. A potential mechanism for cataract formation in vivo involving accumulation of deamidated β-crystallin aggregates is discussed.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Eye Research - Volume 90, Issue 6, June 2010, Pages 688-698
Journal: Experimental Eye Research - Volume 90, Issue 6, June 2010, Pages 688-698
نویسندگان
Magalie Michiel, Elodie Duprat, Fériel Skouri-Panet, Jason A. Lampi, Annette Tardieu, Kirsten J. Lampi, Stéphanie Finet,